2017
Axon tension regulates fasciculation/defasciculation through the control of axon shaft zippering
Šmít D, Fouquet C, Pincet F, Zapotocky M, Trembleau A. Axon tension regulates fasciculation/defasciculation through the control of axon shaft zippering. ELife 2017, 6: e19907. PMID: 28422009, PMCID: PMC5478281, DOI: 10.7554/elife.19907.Peer-Reviewed Original Research
2016
Endothelial basement membrane laminin 511 is essential for shear stress response
Di Russo J, Luik A, Yousif L, Budny S, Oberleithner H, Hofschröer V, Klingauf J, van Bavel E, Bakker E, Hellstrand P, Bhattachariya A, Albinsson S, Pincet F, Hallmann R, Sorokin L. Endothelial basement membrane laminin 511 is essential for shear stress response. The EMBO Journal 2016, 36: 183-201. PMID: 27940654, PMCID: PMC5239996, DOI: 10.15252/embj.201694756.Peer-Reviewed Original ResearchConceptsCell-cell adhesion strengthLaminin-511Junctional complexesVE-cadherinIntegrin-mediated interactionsEndothelial basement membrane componentVinculin-positive focal adhesionsCatenin associationFocal adhesionsStress responseCell junctionsMembrane componentsBasement membrane componentsBasement membraneArterial endotheliumCortical stiffnessMechanotransductionPECAM-1Firm anchorageEndothelial basement membraneJunctional associationMembraneConsiderable informationComplexesAdhesionFRAP to Characterize Molecular Diffusion and Interaction in Various Membrane Environments
Pincet F, Adrien V, Yang R, Delacotte J, Rothman JE, Urbach W, Tareste D. FRAP to Characterize Molecular Diffusion and Interaction in Various Membrane Environments. PLOS ONE 2016, 11: e0158457. PMID: 27387979, PMCID: PMC4936743, DOI: 10.1371/journal.pone.0158457.Peer-Reviewed Original ResearchConceptsFluorescence correlation spectroscopySingle-particle trackingCorresponding recovery timeFRAP measurementsDynamics of lipidsDiffusion coefficientCorrelation spectroscopyBrownian motionParticle trackingConfocal microscopeAccurate valuesDiffusive speciesMembrane environmentMolecular diffusionMeasurementsMembrane platformsBehavior of lipidsFRAP experimentsMotion
2014
Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 accumulation in the intercellular contact area prior to fusion during mammalian fertilization
Chalbi M, Barraud-Lange V, Ravaux B, Howan K, Rodriguez N, Soule P, Ndzoudi A, Boucheix C, Rubinstein E, Wolf J, Ziyyat A, Perez E, Pincet F, Gourier C. Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 accumulation in the intercellular contact area prior to fusion during mammalian fertilization. Development 2014, 141: 3732-3739. PMID: 25209248, DOI: 10.1242/dev.111534.Peer-Reviewed Original ResearchConceptsGamete fusionMammalian fertilizationMolecular mechanismsSperm protein IZUMO1Intercellular contact areaFusion machineryMembrane proteinsMembrane organizationIZUMO1Intercellular adhesionAdhesion partnersRecruitment kineticsKey playersCD9Adhesion phaseEggsAdhesion areaFertilizationFusionHuman eggsGametesMachineryAdhesionSpeciesProteinA Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion
Li F, Kümmel D, Coleman J, Reinisch KM, Rothman JE, Pincet F. A Half-Zippered SNARE Complex Represents a Functional Intermediate in Membrane Fusion. Journal Of The American Chemical Society 2014, 136: 3456-3464. PMID: 24533674, PMCID: PMC3985920, DOI: 10.1021/ja410690m.Peer-Reviewed Original ResearchConceptsN-terminal domainMembrane fusionV-SNARET-SNAREsRecent biophysical studiesC-terminal portionSNARE complexTransmembrane domainRegulatory proteinsFunctional intermediatesC-terminusDistinct functionsN-terminusMolecular mechanismsConformational rearrangementsBiophysical studiesVital regulatorZippering mechanismRate-limiting stepBiological membranesSnareFusionComplexinMultiple stagesZipperingArf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting
Wilfling F, Thiam AR, Olarte MJ, Wang J, Beck R, Gould TJ, Allgeyer ES, Pincet F, Bewersdorf J, Farese RV, Walther TC. Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. ELife 2014, 3: e01607. PMID: 24497546, PMCID: PMC3913038, DOI: 10.7554/elife.01607.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation Factor 1AnimalsBiological TransportCell LineCoat Protein Complex ICOP-Coated VesiclesDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumHumansLipaseLipid DropletsLipolysisMiceNanoparticlesParticle SizePhospholipidsRNA InterferenceSurface TensionTime FactorsTransfectionTriglyceridesConceptsCellular lipid dropletsLipid dropletsProtein machineryProtein targetingUbiquitous organellesVesicle traffickingLD surfaceSpecific proteinsKey enzymeLD morphologyMembrane precursorsMachineryMetabolic energyProteinNeutral lipidsTG storageEnzymeUnclear mechanismsAmount of phospholipidsRecent evidenceOrganellesCOPITraffickingTriacylglycerolsBuds
2013
Homotypic and Heterotypic Adhesion Induced by Odorant Receptors and the β2-Adrenergic Receptor
Richard M, Jamet S, Fouquet C, Dubacq C, Boggetto N, Pincet F, Gourier C, Trembleau A. Homotypic and Heterotypic Adhesion Induced by Odorant Receptors and the β2-Adrenergic Receptor. PLOS ONE 2013, 8: e80100. PMID: 24312457, PMCID: PMC3846556, DOI: 10.1371/journal.pone.0080100.Peer-Reviewed Original ResearchConceptsG protein-coupled receptorsΒ2-adrenergic receptorOlfactory axonsAxon sortingOlfactory sensory neuron projectionsSensory neuron projectionsSubpopulation of axonsMouse olfactory systemOdorant receptorsProtein-coupled receptorsHeterotypic adhesionSensory neuronsAdrenergic receptorsAxonal wiringNeuron projectionsAxonsReceptorsOlfactory systemMOR256-17First evidenceCritical determinant
2012
SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open
Shi L, Shen QT, Kiel A, Wang J, Wang HW, Melia TJ, Rothman JE, Pincet F. SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open. Science 2012, 335: 1355-1359. PMID: 22422984, PMCID: PMC3736847, DOI: 10.1126/science.1214984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumDiffusionLipid BilayersLiposomesMembrane FusionMembrane ProteinsMiceNeurotransmitter AgentsProtein Structure, TertiaryProteolipidsRatsRecombinant Fusion ProteinsSNARE ProteinsSynaptic TransmissionSynaptic VesiclesSynaptosomal-Associated Protein 25Syntaxin 1Vesicle-Associated Membrane Protein 2ConceptsVesicle-associated membrane protein 2Bilayer fusionNative transmembrane domainNascent fusion poresLipid bilayer nanodiscsMembrane protein 2Synchronous neurotransmitter releaseSNARE complexTransmembrane helicesTransmembrane domainBilayer nanodiscsFused bilayersFusion porePore opensFusion partnerBiochemical studiesProtein 2Neurotransmitter releaseNanodiscsSnareEfficient releaseSynaptic transmissionSNAREpinsFusionRelevant time scales
2011
Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state
Li F, Pincet F, Perez E, Giraudo CG, Tareste D, Rothman JE. Complexin activates and clamps SNAREpins by a common mechanism involving an intermediate energetic state. Nature Structural & Molecular Biology 2011, 18: 941-946. PMID: 21785413, PMCID: PMC3736826, DOI: 10.1038/nsmb.2102.Peer-Reviewed Original ResearchCD9 tetraspanin generates fusion competent sites on the egg membrane for mammalian fertilization
Jégou A, Ziyyat A, Barraud-Lange V, Perez E, Wolf J, Pincet F, Gourier C. CD9 tetraspanin generates fusion competent sites on the egg membrane for mammalian fertilization. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 10946-10951. PMID: 21690351, PMCID: PMC3131345, DOI: 10.1073/pnas.1017400108.Peer-Reviewed Original ResearchConceptsAdhesion sitesFusion-competent sitesWild-type eggsCD9 tetraspaninEgg membrane proteinsSperm-egg fusionMembrane proteinsGamete membranesMammalian fertilizationCompetent sitesGamete interactionAdhesion eventsTight proximityEgg membraneCD9TetraspaninsEggsFertilizationMembraneStrong-interaction modesAdhesion probabilitySitesFusionInteraction modesProtein
2010
Integrins stimulate E-cadherin-mediated intercellular adhesion by regulating Src-kinase activation and actomyosin contractility
Martinez-Rico C, Pincet F, Thiery JP, Dufour S. Integrins stimulate E-cadherin-mediated intercellular adhesion by regulating Src-kinase activation and actomyosin contractility. Journal Of Cell Science 2010, 123: 712-722. PMID: 20144995, DOI: 10.1242/jcs.047878.Peer-Reviewed Original ResearchConceptsIntercellular adhesionActomyosin contractilityCell doubletsE-cadherin-mediated intercellular adhesionIntercellular adhesion strengthSrc family kinasesCell-matrix interactionsSrc kinase activationExistence of crosstalkRole of integrinsFamily kinasesCadherin-7Cell plasticityMolecular crosstalkMajor adhesion moleculeIntegrin stimulationCell spreadingCadherinCell adhesionII activityIntegrinsPolylysine-coated beadsAdhesion moleculesCrosstalkAdhesion
2007
Mapping Mouse Gamete Interaction Forces Reveal Several Oocyte Membrane Regions with Different Mechanical and Adhesive Properties †
Jégou A, Pincet F, Perez E, Wolf JP, Ziyyat A, Gourier C. Mapping Mouse Gamete Interaction Forces Reveal Several Oocyte Membrane Regions with Different Mechanical and Adhesive Properties †. Langmuir 2007, 24: 1451-1458. PMID: 18027975, DOI: 10.1021/la702258x.Peer-Reviewed Original ResearchEnergetics and dynamics of SNAREpin folding across lipid bilayers
Li F, Pincet F, Perez E, Eng WS, Melia TJ, Rothman JE, Tareste D. Energetics and dynamics of SNAREpin folding across lipid bilayers. Nature Structural & Molecular Biology 2007, 14: 890-896. PMID: 17906638, DOI: 10.1038/nsmb1310.Peer-Reviewed Original Research
2005
Johnson-Kendall-Roberts Theory Applied to Living Cells
Chu YS, Dufour S, Thiery JP, Perez E, Pincet F. Johnson-Kendall-Roberts Theory Applied to Living Cells. Physical Review Letters 2005, 94: 028102. PMID: 15698233, DOI: 10.1103/physrevlett.94.028102.Peer-Reviewed Original Research
2004
Force measurements in E-cadherin–mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42
Chu Y, Thomas W, Eder O, Pincet F, Perez E, Thiery J, Dufour S. Force measurements in E-cadherin–mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42. Journal Of Cell Biology 2004, 167: 1183-1194. PMID: 15596540, PMCID: PMC2172605, DOI: 10.1083/jcb.200403043.Peer-Reviewed Original ResearchConceptsActin cytoskeletonCadherin-dependent cell-cell adhesionE-cadherin-based adhesionsE-cadherin-expressing cellsCell adhesionActin cytoskeleton dynamicsRho-like small GTPasesCell-cell adhesionDominant active formDominant-negative formStrong cell adhesionFunctional cadherinCytoskeleton dynamicsSmall GTPasesCell doubletsHomophilic interactionsActin polymerizationIntercellular adhesionCdc42Negative formCadherinCell surfaceCadherin levelsCytoskeletonRacSeparation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3*
Martinez-Rico C, Pincet F, Perez E, Thiery J, Shimizu K, Takai Y, Dufour S. Separation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3*. Journal Of Biological Chemistry 2004, 280: 4753-4760. PMID: 15550395, DOI: 10.1074/jbc.m412544200.Peer-Reviewed Original ResearchConceptsE-cadherin-based adhesionsNectin-3E-cadherin-dependent cell adhesionExtracellular fragmentE-cadherin-mediated adhesionE-cadherin-expressing cellsNectin-1Cell adhesionCell-cell adhesionIndependent cell adhesion moleculesAdherens junctionsCell adhesion moleculeCell doubletsSignificant agonistic effectKey moleculesE-cadherinL cellsCadherinNectinAdhesion moleculesCellsAdhesionFragmentsHomodimerHeterodimers